We have constructed (and continue to develop) a laser-based facility for time-resolved fluorescence spectroscopy of biomolecules. This facility provides rapid collection and analysis of luminescence data related to macromolecular size, flexibility, folding and structural fluctuations. Our time-correlated laser fluorometer was used to study the folding and dynamics of several proteins. Cloned fragments of soluble CD4, the initial binding target for HIV, were studied to see if bacterial expression provided usable "decoy" structures. Unfortunately, the fragments was found to cluster into 'useless' hexamers (this measurement 'cut off' an unproductive line of genetic engineering). We studied several DNA-binding proteins. We found that the fluorescence of endonuclease BamHl was quenched in a way suggesting the DNA-bound form had an altered shape. In particular, anisotropy studies showed the BamHl had 'condensed' around the recognition region (e.g., lost hydrodynamic volume). We are conducting similar studies with TFIIIA (a 'zinc finger' protein), beta polymerase, and transactivating factor 'pou'. We published new methods for examining the interaction of peptides with lipid bilayers. Our studies of influenza virus found that the pH driven 'fusion trigger' is a local structural change that does not alter the depth (or rigidity) of protein-lipid contacts. We are continuing similar studies with 'leader peptides'. We published new data analysis methods for kinetic data, uniquely adapting a method known as "simulated annealing". This year we also initiated efforts to adapt our laser instruments to the imaging of tissues. Tissue diffuses even red light rapidly, but our subnanosecond timing lets us examine the "shock wave" of brightness engulfing tissues. This may lead to practical, noninvasive tissue imaging devices in the future that compete with MR1.